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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 613 (1990), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Bioprocess and biosystems engineering 5 (1990), S. 31-38 
    ISSN: 1432-0797
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Heat conditioning of cell homogenates of B. cereus and a recombinant E. coli was studied for the isolation of leucine dehydrogenase and alanine racemase, respectively. The strain of E. coli carried the gene of the thermostable alanine racemase from B. stearothermophilus. Activity loss can be minimized (〈5%) and aggregation and flocculation of soluble proteins (70–80%) and other cell components can be achieved, depending on temperature, biomass concentration and pH-value. Thereby a 3–6 fold increase in specific activity was obtained. The resulting extract after solid-liquid separation showed lower viscosity and less turbidity than unheated controls, making it more suitable for chromatographic separations.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Bioprocess and biosystems engineering 6 (1991), S. 173-177 
    ISSN: 1432-0797
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The costs for the recycling of salt from the primary bottom phase are estimated in a protein extraction process. The extraction of 1 kg potassium phosphate in a phase system formed in the presence of ethanol costs approximately 6 to 7 DM. This is within the same order as for the cost resulting from the purchase price of 3 DM/kgsalt and the additional costs for deposition of the primary bottom phase. A mathematical description of the cost structure is developed and allows to estimate cost for various conditions.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 34 (1990), S. 287-291 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A fructose 1,6-bisphosphate aldolase (E.C.4.1.2.13) from Staphylococcus carnosus DSM 20501 was purified for the first time. The enzymatic activity was insensitive to high levels of EDTA indicating that the enzyme is a class I aldolase. This enzyme exhibits good stability at high temperatures and extreme stability over a wide pH range. The K m for fructose 1,6-bisphosphate as substrate was 0.022 mm. The S. carnosus aldolase is a monomeric enzyme with a molecular mass of about 33 kDa. It exhibits a relatively broad pH optimum between pH 6.5 and 9.0. Furthermore, the aldolase accepts other aldehydes in place of its natural substrate, glyceraldehyde 3-phosphate, allowing the synthesis of various sugar phosphates.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Chemie in unserer Zeit 26 (1992), S. V 
    ISSN: 0009-2851
    Keywords: Chemistry ; Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 986-994 
    ISSN: 0006-3592
    Keywords: protein partitioning ; polyethyleneglycol/dextran systems ; isoelectric point ; polymer molecular weight ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: We report the partition coefficient, Kp′ at the isoelectric point of lysozyme, chymotrypsinogen A, albumin, transferrin, and catalase in 64 different polyethylene(PEG)/ dextran(Dx)/water systems. We study the trends of the partition coefficient with protein type, polymer concentration, and polymer molecular weight. We find that the partition coefficient decreases with increasing tie line length for lysozyme, albumin, transferrin, and catalase for which Kp is less than 1, but increases for chymotrysinogen for which Kp is larger than 1. The effect of the tie line length on the partition coefficient is larger for the large proteins than for the small proteins. The partition coefficient decreases with increasing protein molecular weight except for lysozyme suggesting that lysozyme is present as a dimer or a trimer. The partition coefficient decreases with increasing PEG molecular weight, but the magnitude of the increase is larger for the smaller PEG molecular eights and tends to level of at high PEG molecular weight. The partition coefficient increases with increasing dextran (Dx) molecular weight for chymotrypsinogen but decreases for catalase. The partition coefficients of lysozyme, albumin, and transferrin increase with increasing Dx molecular weight from Dx 104 to Dx 1.1 × 105 and then slightly decrease from Dx 1.1 × 105 to Dx 5 × 105. The experimental results are analyzed using a statistical thermodynamics model. The experimental results are analyzed using a statistical thermodynamics model. The experiments suggest that protein partitioning at the isoelectric point in aqueous two-phase systems is strongly related to the size of the proteins and polymers. Finally, the impossibility of obtaining data completely independent of polymer concentration is emphasized.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 132-140 
    ISSN: 0006-3592
    Keywords: enzymatic synthesis ; continuous production ; anion-exchange ; peptide-amidase ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A simple system is introduced to produce dipeptides continuously by enzyme catalyzed condensation of amino acid esters and amino acid amides. Synthesis of N-terminal free dipeptide-amides is achieved by means of carboxypeptidase Y. The peptide-amide is deamidated utilizing a newly isolated peptide-amide is deamidated utilizing a newly isolated peptide-amidase. Separation of substrates and products is accomplished by anion-exchange chromatography. Modeling of the reactions shows that the two reactions have to be carried out in a cascade of two reactors in order to prevent hydrolysis of the peptide by the carboxypeptidase. Continuous production of Kyotorphin (H-TyrArg-OH) with a space-time yield of 257 g/L · d shows the feasibility of this concept.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 33-40 
    ISSN: 0006-3592
    Keywords: downstream ; purification ; dye-ligand ; affinity membranes ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A new adsorbent for the selective binding of enzymes, in the form of microporous membranes carrying triazine dyes as pseudo-affinity ligand, has been implemented in the recovery of glucose-6-phosphate dehydrogenase from yeast. A detailed investigation of the process parameters has been performed. In the adsorption step, the contact time for binding G6PDH could be reduced down to 0.25 s without significant decrease of the capture efficiency. Hence, fast filtration allowed to isolate G6PDH from a dilute extract (1.6 μg G6PDH · mL-1), where the enzyme accounted for 1% of the proteins. The yield of the selective elution step using NADP was only 70% at best. It could be improved to near 100% by supplementing the eluent with ethylene glycol, without loss of selectivity. A Scale-up of the cross-section of the membrane by a factor of 40 allowed to purify 1140 U from 0.6 L extract from 1% to 57% purity with 82% yield, within 10 minutes. The case study presented here demonstrates the applicability of general-purpose membrane adsorbents for the purification of enzymes.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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